ID   LYSE_DROME              Reviewed;         140 AA.
AC   P37159; C9QP86; Q8MS67; Q9W0J5;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 2.
DT   27-MAR-2024, entry version 162.
DE   RecName: Full=Lysozyme E;
DE            EC=3.2.1.17;
DE   AltName: Full=1,4-beta-N-acetylmuramidase E;
DE   Flags: Precursor;
GN   Name=LysE; ORFNames=CG1180;
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Canton-S;
RX   PubMed=8159165; DOI=10.1007/bf00391008;
RA   Daffre S., Kylsten P., Samakovlis C., Hultmark D.;
RT   "The lysozyme locus in Drosophila melanogaster: an expanded gene family
RT   adapted for expression in the digestive tract.";
RL   Mol. Gen. Genet. 242:152-162(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley;
RX   PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA   Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA   Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA   George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA   Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA   Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA   Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA   An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA   Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA   Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA   Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA   Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA   Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA   Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA   Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA   Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA   Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA   Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA   Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA   Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA   Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA   Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA   McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA   Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA   Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA   Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA   Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA   Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA   Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA   Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA   Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA   Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA   Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA   Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA   Venter J.C.;
RT   "The genome sequence of Drosophila melanogaster.";
RL   Science 287:2185-2195(2000).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=Berkeley;
RX   PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA   Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA   Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA   Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA   Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA   Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA   Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT   review.";
RL   Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Berkeley; TISSUE=Larva, and Pupae;
RA   Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Booth B.,
RA   Champe M., Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E.,
RA   George R.A., Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G.,
RA   Miranda A., Mungall C.J., Nunoo J., Pacleb J., Paragas V., Park S.,
RA   Patel S., Phouanenavong S., Sandler J., Wan K.H., Yu C., Lewis S.E.,
RA   Rubin G.M., Celniker S.E.;
RL   Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Unlikely to play an active role in the humoral immune
CC       defense. May have a function in the digestion of bacteria in the food.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of (1->4)-beta-linkages between N-acetylmuramic
CC         acid and N-acetyl-D-glucosamine residues in a peptidoglycan and
CC         between N-acetyl-D-glucosamine residues in chitodextrins.;
CC         EC=3.2.1.17;
CC   -!- TISSUE SPECIFICITY: Found in the midgut.
CC   -!- DEVELOPMENTAL STAGE: Maximal expression is found during the third
CC       larval instar, it drops to become undetectable in the late pupal stage.
CC       The expression in adults is similar to that of first and second larval
CC       instars.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 22 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00680}.
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DR   EMBL; Z22227; CAA80229.1; -; Genomic_DNA.
DR   EMBL; AE014296; AAF47451.1; -; Genomic_DNA.
DR   EMBL; AY119059; AAM50919.1; -; mRNA.
DR   EMBL; BT099968; ACX53649.1; -; mRNA.
DR   PIR; S41577; S41577.
DR   RefSeq; NP_476827.2; NM_057479.3.
DR   AlphaFoldDB; P37159; -.
DR   SMR; P37159; -.
DR   BioGRID; 63674; 1.
DR   DIP; DIP-20170N; -.
DR   STRING; 7227.FBpp0072526; -.
DR   CAZy; GH22; Glycoside Hydrolase Family 22.
DR   PaxDb; 7227-FBpp0072526; -.
DR   DNASU; 38128; -.
DR   EnsemblMetazoa; FBtr0072630; FBpp0072526; FBgn0004428.
DR   GeneID; 38128; -.
DR   KEGG; dme:Dmel_CG1180; -.
DR   AGR; FB:FBgn0004428; -.
DR   CTD; 38128; -.
DR   FlyBase; FBgn0004428; LysE.
DR   VEuPathDB; VectorBase:FBgn0004428; -.
DR   eggNOG; ENOG502S1S1; Eukaryota.
DR   GeneTree; ENSGT00940000166760; -.
DR   HOGENOM; CLU_111620_2_1_1; -.
DR   InParanoid; P37159; -.
DR   OMA; SAANWIC; -.
DR   OrthoDB; 5361006at2759; -.
DR   PhylomeDB; P37159; -.
DR   Reactome; R-DME-5653890; Lactose synthesis.
DR   BioGRID-ORCS; 38128; 0 hits in 3 CRISPR screens.
DR   GenomeRNAi; 38128; -.
DR   PRO; PR:P37159; -.
DR   Proteomes; UP000000803; Chromosome 3L.
DR   Bgee; FBgn0004428; Expressed in midgut and 11 other cell types or tissues.
DR   GO; GO:0005615; C:extracellular space; ISS:FlyBase.
DR   GO; GO:0003796; F:lysozyme activity; ISS:FlyBase.
DR   GO; GO:0050829; P:defense response to Gram-negative bacterium; HMP:FlyBase.
DR   GO; GO:0031640; P:killing of cells of another organism; IEA:UniProtKB-KW.
DR   GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0045824; P:negative regulation of innate immune response; HMP:FlyBase.
DR   CDD; cd16899; LYZ_C_invert; 1.
DR   Gene3D; 1.10.530.10; -; 1.
DR   InterPro; IPR001916; Glyco_hydro_22.
DR   InterPro; IPR019799; Glyco_hydro_22_CS.
DR   InterPro; IPR000974; Glyco_hydro_22_lys.
DR   InterPro; IPR023346; Lysozyme-like_dom_sf.
DR   PANTHER; PTHR11407:SF36; GEO02684P1-RELATED; 1.
DR   PANTHER; PTHR11407; LYSOZYME C; 1.
DR   Pfam; PF00062; Lys; 1.
DR   PRINTS; PR00137; LYSOZYME.
DR   PRINTS; PR00135; LYZLACT.
DR   SMART; SM00263; LYZ1; 1.
DR   SUPFAM; SSF53955; Lysozyme-like; 1.
DR   PROSITE; PS00128; GLYCOSYL_HYDROL_F22_1; 1.
DR   PROSITE; PS51348; GLYCOSYL_HYDROL_F22_2; 1.
PE   2: Evidence at transcript level;
KW   Antimicrobial; Bacteriolytic enzyme; Disulfide bond; Glycosidase;
KW   Hydrolase; Reference proteome; Signal.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000250"
FT   CHAIN           19..140
FT                   /note="Lysozyme E"
FT                   /id="PRO_0000018513"
FT   DOMAIN          19..140
FT                   /note="C-type lysozyme"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT   ACT_SITE        50
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT   ACT_SITE        68
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT   DISULFID        24..139
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT   DISULFID        45..129
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT   DISULFID        80..96
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT   DISULFID        92..110
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT   CONFLICT        12
FT                   /note="M -> L (in Ref. 1; CAA80229)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        76
FT                   /note="N -> D (in Ref. 1; CAA80229)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        138
FT                   /note="G -> D (in Ref. 1; CAA80229)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   140 AA;  15553 MW;  CEB5465CF6B6F123 CRC64;
     MKAFIVLVAL AMAAPALGRT LDRCSLAREM SNLGVPRDQL ARWACIAEHE SSYRTGVVGP
     ENYNGSNDYG IFQINNYYWC APPSGRFSYN ECGLSCNALL TDDITHSVRC AQKVLSQQGW
     SAWSTWHYCS GWLPSIDGCF
//